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10.1038/s41467-021-23533-x http://scihub22266oqcxt.onion/10.1038/s41467-021-23533-x 34103506!8187709!34103506     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2021 ; 12 (1): 3433 Nephropedia Template TP {{tp|p=34103506|t=2021. Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1 |pdf=|usr=}}{{34103506}} gab.com Text Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1 JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34103506 #FOAvip The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which occurs through viral protein recognition of human targets. To understand the structural basis for SARS-CoV-2 viral-host protein recognition, here we use cryo-electron microscopy (cryo-EM) to determine a complex structure of the human cell junction protein PALS1 and SARS-CoV-2 viral envelope (E) protein. Our reported structure shows that the E protein C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains of PALS1. Our structural analysis provides an explanation for the observation that the viral E protein recruits PALS1 from lung epithelial cell junctions. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1-E interactions to reduce E-mediated virulence. Twit Text FOAVip Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1 ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34103506 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34103506 #FOAvip English Wikipedia <ref>{{Cite pmid|34103506}}</ref> Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1 #MMPMID34103506 Chai J; Cai Y; Pang C; Wang L; McSweeney S; Shanklin J; Liu Q Nat Commun 2021[Jun]; 12 (1): 3433 PMID34103506show ga The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which occurs through viral protein recognition of human targets. To understand the structural basis for SARS-CoV-2 viral-host protein recognition, here we use cryo-electron microscopy (cryo-EM) to determine a complex structure of the human cell junction protein PALS1 and SARS-CoV-2 viral envelope (E) protein. Our reported structure shows that the E protein C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains of PALS1. Our structural analysis provides an explanation for the observation that the viral E protein recruits PALS1 from lung epithelial cell junctions. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1-E interactions to reduce E-mediated virulence. |Amino Acid Sequence[MESH] |Coronavirus Envelope Proteins/*chemistry/*metabolism/ultrastructure[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Intercellular Junctions/*metabolism[MESH] |Membrane Proteins/*metabolism[MESH] |Nucleoside-Phosphate Kinase/*metabolism[MESH] |Protein Domains[MESH] |SARS-CoV-2/physiology[MESH] |Structural Homology, Protein[MESH]Structural basis for SARS-CoV-2 envelope protein recognition of human (epmc).pdf DeepDyve Pubget Overpricing